Ultrathin porous PdCu metallenezymes as oxidase mimics for colorimetric analysis

Enzyme Mimetic Activity of Intercalated Pd–H Nanosheets for Bioanalysis

“…Additionally, the NSAs reveal excellent storage stability, retaining 98% of their activity even after 100 days (Figure S3f). Comparison to some previous literature 16,19 showed that the V max value of Pd−H NSAs is higher than that of other Pdbased nanozymes (Table S3). Moreover, the K cat (26.43 s −1 ) and K cat /K m (50.83 s −1 ) are dramatically higher than those of Pd NSAs and some of the previously reported Pd-based nanozymes (Table S3).…”

“…Macromolecular biocatalysts, named enzymes found in living organisms and mainly composed of proteins, are responsible for regulating the possible chemical reactions in living organisms . Owing to their high substrate specificity and catalytic activity, natural enzymes have been extensively used in biological fields, industry, medicines, etc. − However, their low stability, high cost, and complex production process increase the demand for artificial enzymes, which are proven to be promising candidates in the fields of nanotechnology, , biotechnology, , and nanomaterials science. , Enzyme-like activities of nanozymes, such as oxidase-like, − peroxidase-like, − and catalase-like, , have been explored through various studies. Furthermore, nanozymes have been explored for the antibacterial activity at physiological pH in the presence of adenosine triphosphate (ATP) .…”